ID KIF17_HUMAN Reviewed; 1029 AA. AC Q9P2E2; A2A3Q7; A2A3Q8; O95077; Q53YS6; Q5VWA9; Q6GSA8; Q8N411; DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2011, sequence version 3. DT 27-MAR-2024, entry version 183. DE RecName: Full=Kinesin-like protein KIF17; DE AltName: Full=KIF3-related motor protein; GN Name=KIF17; Synonyms=KIAA1405, KIF3X; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS MET-402 AND GLU-933. RX PubMed=14673085; DOI=10.1073/pnas.2536695100; RA Chennathukuzhi V., Morales C.R., El-Alfy M., Hecht N.B.; RT "The kinesin KIF17b and RNA-binding protein TB-RBP transport specific cAMP- RT responsive element modulator-regulated mRNAs in male germ cells."; RL Proc. Natl. Acad. Sci. U.S.A. 100:15566-15571(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS MET-402 RP AND GLU-933. RC TISSUE=Eye; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 78-1029 (ISOFORM 1), AND VARIANTS RP MET-402 AND GLU-933. RC TISSUE=Brain; RX PubMed=10718198; DOI=10.1093/dnares/7.1.65; RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XVI. The RT complete sequences of 150 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 7:65-73(2000). RN [5] RP SEQUENCE REVISION. RA Ohara O., Nagase T., Kikuno R.; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 793-1029, AND VARIANT GLU-933. RA Nagata K., Puls A., Futter C., Aspenstroem P., Hall A.; RT "The MAP kinase kinase kinases MLK2 and MLK3 are targets for RAC/Cdc42 and RT components of microtubule motor complexes."; RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Dendrite-specific motor protein which, in association with CC the Apba1-containing complex (LIN-10-LIN-2-LIN-7 complex), transports CC vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit NR2B CC along microtubules. {ECO:0000250|UniProtKB:Q99PW8}. CC -!- SUBUNIT: Homodimer (By similarity). Interacts with APBA1 (via PDZ CC domain); the interaction is direct and is required for association of CC KIF17 with the cargo that is to be transported (By similarity). CC Interacts with IFT B complex components IFT52 and IFT57 (By CC similarity). Interacts with IFT70B (By similarity). Interacts with CC PIWIL1 (By similarity). Interacts with TBATA (By similarity). CC {ECO:0000250|UniProtKB:Q99PW8}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cell CC projection, cilium {ECO:0000250|UniProtKB:Q99PW8}. Cell projection, CC dendrite {ECO:0000250|UniProtKB:Q99PW8}. Note=Localizes to dendrites of CC pyramidal neurons (By similarity). Does not localize to the axons or CC nuclei in cerebral cortex, hippocampus or olfactory bulb (By CC similarity). Co-localizes with NR2B-containing vesicles along CC microtubules (By similarity). {ECO:0000250|UniProtKB:Q99PW8}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=KIF17b; CC IsoId=Q9P2E2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9P2E2-3; Sequence=VSP_040346; CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD01428.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAD01428.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305}; CC Sequence=AAH36871.1; Type=Miscellaneous discrepancy; Note=Cloning artifact.; Evidence={ECO:0000305}; CC Sequence=BAA92643.2; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY484427; AAR33039.1; -; mRNA. DR EMBL; AL391357; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL663074; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC036871; AAH36871.1; ALT_SEQ; mRNA. DR EMBL; BC065927; AAH65927.1; -; mRNA. DR EMBL; AB037826; BAA92643.2; ALT_SEQ; mRNA. DR EMBL; AF009624; AAD01428.1; ALT_SEQ; mRNA. DR CCDS; CCDS213.1; -. [Q9P2E2-1] DR CCDS; CCDS44079.1; -. [Q9P2E2-3] DR RefSeq; NP_001116291.1; NM_001122819.2. [Q9P2E2-3] DR RefSeq; NP_001274141.1; NM_001287212.1. DR RefSeq; NP_065867.2; NM_020816.3. [Q9P2E2-1] DR AlphaFoldDB; Q9P2E2; -. DR SMR; Q9P2E2; -. DR BioGRID; 121629; 7. DR IntAct; Q9P2E2; 8. DR MINT; Q9P2E2; -. DR STRING; 9606.ENSP00000247986; -. DR iPTMnet; Q9P2E2; -. DR PhosphoSitePlus; Q9P2E2; -. DR BioMuta; KIF17; -. DR DMDM; 317373436; -. DR EPD; Q9P2E2; -. DR jPOST; Q9P2E2; -. DR MassIVE; Q9P2E2; -. DR MaxQB; Q9P2E2; -. DR PaxDb; 9606-ENSP00000247986; -. DR PeptideAtlas; Q9P2E2; -. DR ProteomicsDB; 83790; -. [Q9P2E2-1] DR ProteomicsDB; 83791; -. [Q9P2E2-3] DR Antibodypedia; 15106; 153 antibodies from 22 providers. DR DNASU; 57576; -. DR Ensembl; ENST00000247986.2; ENSP00000247986.2; ENSG00000117245.13. [Q9P2E2-1] DR Ensembl; ENST00000400463.8; ENSP00000383311.3; ENSG00000117245.13. [Q9P2E2-3] DR GeneID; 57576; -. DR KEGG; hsa:57576; -. DR MANE-Select; ENST00000400463.8; ENSP00000383311.3; NM_001122819.3; NP_001116291.1. [Q9P2E2-3] DR UCSC; uc001bdr.6; human. [Q9P2E2-1] DR AGR; HGNC:19167; -. DR CTD; 57576; -. DR DisGeNET; 57576; -. DR GeneCards; KIF17; -. DR HGNC; HGNC:19167; KIF17. DR HPA; ENSG00000117245; Tissue enriched (testis). DR MIM; 605037; gene. DR neXtProt; NX_Q9P2E2; -. DR OpenTargets; ENSG00000117245; -. DR PharmGKB; PA38809; -. DR VEuPathDB; HostDB:ENSG00000117245; -. DR eggNOG; KOG0239; Eukaryota. DR GeneTree; ENSGT00940000158776; -. DR HOGENOM; CLU_001485_22_0_1; -. DR InParanoid; Q9P2E2; -. DR OMA; AKNRMVG; -. DR OrthoDB; 5481713at2759; -. DR PhylomeDB; Q9P2E2; -. DR TreeFam; TF105223; -. DR PathwayCommons; Q9P2E2; -. DR Reactome; R-HSA-5620924; Intraflagellar transport. DR Reactome; R-HSA-9609736; Assembly and cell surface presentation of NMDA receptors. DR SignaLink; Q9P2E2; -. DR SIGNOR; Q9P2E2; -. DR BioGRID-ORCS; 57576; 15 hits in 1149 CRISPR screens. DR GeneWiki; KIF17; -. DR GenomeRNAi; 57576; -. DR Pharos; Q9P2E2; Tbio. DR PRO; PR:Q9P2E2; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9P2E2; Protein. DR Bgee; ENSG00000117245; Expressed in left testis and 103 other cell types or tissues. DR ExpressionAtlas; Q9P2E2; baseline and differential. DR GO; GO:0005930; C:axoneme; IEA:Ensembl. DR GO; GO:0036064; C:ciliary basal body; IEA:Ensembl. DR GO; GO:0005929; C:cilium; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0032839; C:dendrite cytoplasm; IEA:GOC. DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central. DR GO; GO:0005874; C:microtubule; IBA:GO_Central. DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central. DR GO; GO:0043005; C:neuron projection; IBA:GO_Central. DR GO; GO:1990075; C:periciliary membrane compartment; IEA:Ensembl. DR GO; GO:0032391; C:photoreceptor connecting cilium; IEA:Ensembl. DR GO; GO:0001917; C:photoreceptor inner segment; IEA:Ensembl. DR GO; GO:0001750; C:photoreceptor outer segment; IEA:Ensembl. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central. DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central. DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central. DR GO; GO:0098971; P:anterograde dendritic transport of neurotransmitter receptor complex; IBA:GO_Central. DR GO; GO:0030030; P:cell projection organization; IBA:GO_Central. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0016192; P:vesicle-mediated transport; IEA:Ensembl. DR Gene3D; 3.40.850.10; Kinesin motor domain; 1. DR InterPro; IPR027640; Kinesin-like_fam. DR InterPro; IPR019821; Kinesin_motor_CS. DR InterPro; IPR001752; Kinesin_motor_dom. DR InterPro; IPR036961; Kinesin_motor_dom_sf. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR47969; CHROMOSOME-ASSOCIATED KINESIN KIF4A-RELATED; 1. DR PANTHER; PTHR47969:SF32; KINESIN-LIKE PROTEIN; 1. DR Pfam; PF00225; Kinesin; 1. DR PRINTS; PR00380; KINESINHEAVY. DR SMART; SM00129; KISc; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00411; KINESIN_MOTOR_1; 1. DR PROSITE; PS50067; KINESIN_MOTOR_2; 1. DR Genevisible; Q9P2E2; HS. PE 2: Evidence at transcript level; KW Alternative splicing; ATP-binding; Cell projection; Coiled coil; Cytoplasm; KW Cytoskeleton; Microtubule; Motor protein; Nucleotide-binding; KW Protein transport; Reference proteome; Transport. FT CHAIN 1..1029 FT /note="Kinesin-like protein KIF17" FT /id="PRO_0000125450" FT DOMAIN 5..335 FT /note="Kinesin motor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283" FT REGION 523..569 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 647..673 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 908..931 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 968..1029 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 346..462 FT /evidence="ECO:0000255" FT COILED 739..846 FT /evidence="ECO:0000255" FT COMPBIAS 532..549 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 657..673 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 968..992 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1010..1029 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 91..98 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283" FT VAR_SEQ 908 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_040346" FT VARIANT 341 FT /note="I -> V (in dbSNP:rs2296225)" FT /id="VAR_055983" FT VARIANT 369 FT /note="S -> R (in dbSNP:rs56750936)" FT /id="VAR_061282" FT VARIANT 402 FT /note="V -> M (in dbSNP:rs522496)" FT /evidence="ECO:0000269|PubMed:10718198, FT ECO:0000269|PubMed:14673085, ECO:0000269|PubMed:15489334" FT /id="VAR_023527" FT VARIANT 675 FT /note="V -> I (in dbSNP:rs558760)" FT /id="VAR_055984" FT VARIANT 735 FT /note="V -> I (in dbSNP:rs13375609)" FT /id="VAR_055985" FT VARIANT 933 FT /note="D -> E (in dbSNP:rs631357)" FT /evidence="ECO:0000269|PubMed:10718198, FT ECO:0000269|PubMed:14673085, ECO:0000269|PubMed:15489334, FT ECO:0000269|Ref.6" FT /id="VAR_023528" FT CONFLICT 925 FT /note="D -> Y (in Ref. 6; AAD01428)" FT /evidence="ECO:0000305" FT CONFLICT 957 FT /note="R -> W (in Ref. 1; AAR33039 and 4; BAA92643)" FT /evidence="ECO:0000305" SQ SEQUENCE 1029 AA; 115068 MW; ED1B7F9806CC9AF6 CRC64; MASEAVKVVV RCRPMNQRER ELRCQPVVTV DCARAQCCIQ NPGAADEPPK QFTFDGAYHV DHVTEQIYNE IAYPLVEGVT EGYNGTIFAY GQTGSGKSFT MQGLPDPPSQ RGIIPRAFEH VFESVQCAEN TKFLVRASYL EIYNEDVRDL LGADTKQKLE LKEHPEKGVY VKGLSMHTVH SVAQCEHIME TGWKNRSVGY TLMNKDSSRS HSIFTISIEM SAVDERGKDH LRAGKLNLVD LAGSERQSKT GATGERLKEA TKINLSLSAL GNVISALVDG RCKHVPYRDS KLTRLLQDSL GGNTKTLMVA CLSPADNNYD ETLSTLRYAN RAKNIRNKPR INEDPKDALL REYQEEIKKL KAILTQQMSP SSLSALLSRQ VPPDPVQVEE KLLPQPVIQH DVEAEKQLIR EEYEERLARL KADYKAEQES RARLEEDITA MRNSYDVRLS TLEENLRKET EAVLQVGVLY KAEVMSRAEF ASSAEYPPAF QYETVVKPKV FSTTDTLPSD DVSKTQVSSR FAELPKVEPS KSEISLGSSE SSSLEETSVS EAFPGPEEPS NVEVSMPTEE SRSRYFLDEC LGQEAAGHLL GEQNYLPQEE PQEVPLQGLL GLQDPFAEVE AKLARLSSTV ARTDAPQADV PKVPVQVPAP TDLLEPSDAR PEAEAADDFP PRPEVDLASE VALEVVRTAE PGVWLEAQAP VALVAQPEPL PATAGVKRES VGMEVAVLTD DPLPVVDQQQ VLARLQLLEQ QVVGGEQAKN KDLKEKHKRR KRYADERRKQ LVAALQNSDE DSGDWVLLNV YDSIQEEVRA KSKLLEKMQR KLRAAEVEIK DLQSEFQLEK IDYLATIRRQ ERDSMLLQQL LEQVQPLIRR DCNYSNLEKI LRESCWDEDN GFWKIPHPVI TKTSLPVAVS TGPQNKPARK TSAADNGEPN MEDDRYRLML SRSNSENIAS NYFRSKRASQ ILSTDARKSL THHNSPPGLS CPLSNNSAIP PTQAPEMPQP RPFRLESLDI PFTKAKRKKS KSNFGSEPL //